MMSA_BOVIN
ID MMSA_BOVIN Reviewed; 537 AA.
AC Q07536;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial;
DE Short=MMSDH;
DE Short=Malonate-semialdehyde dehydrogenase [acylating];
DE EC=1.2.1.18 {ECO:0000269|PubMed:8514806};
DE EC=1.2.1.27 {ECO:0000269|PubMed:8514806};
DE AltName: Full=Aldehyde dehydrogenase family 6 member A1;
DE Flags: Precursor;
GN Name=ALDH6A1; Synonyms=MMSDH;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Liver;
RX PubMed=8514806; DOI=10.1016/s0021-9258(18)86919-8;
RA Deichaite I., Berthiaume L., Peseckis S.M., Patton W.F., Resh M.D.;
RT "Novel use of an iodo-myristyl-CoA analog identifies a semialdehyde
RT dehydrogenase in bovine liver.";
RL J. Biol. Chem. 268:13738-13747(1993).
CC -!- FUNCTION: Plays a role in valine and pyrimidine metabolism. Binds fatty
CC acyl-CoA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) +
CC hydrogencarbonate + NADH + propanoyl-CoA; Xref=Rhea:RHEA:20804,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57700, ChEBI:CHEBI:57945; EC=1.2.1.27;
CC Evidence={ECO:0000269|PubMed:8514806};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxopropanoate + CoA + NAD(+) = acetyl-CoA + CO2 + NADH;
CC Xref=Rhea:RHEA:22992, ChEBI:CHEBI:16526, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.18;
CC Evidence={ECO:0000269|PubMed:8514806};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxopropanoate + CoA + NADP(+) = acetyl-CoA + CO2 + NADPH;
CC Xref=Rhea:RHEA:22988, ChEBI:CHEBI:16526, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.18;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; L08643; AAA30650.1; -; mRNA.
DR PIR; A46600; A46600.
DR RefSeq; NP_787005.1; NM_175811.2.
DR AlphaFoldDB; Q07536; -.
DR SMR; Q07536; -.
DR STRING; 9913.ENSBTAP00000024584; -.
DR PaxDb; Q07536; -.
DR PeptideAtlas; Q07536; -.
DR PRIDE; Q07536; -.
DR GeneID; 327692; -.
DR KEGG; bta:327692; -.
DR CTD; 4329; -.
DR eggNOG; KOG2449; Eukaryota.
DR InParanoid; Q07536; -.
DR OrthoDB; 608999at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:UniProtKB.
DR GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; ISS:UniProtKB.
DR GO; GO:0102662; F:malonate-semialdehyde dehydrogenase (acetylating, NAD+) activity; IEA:RHEA.
DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; IDA:UniProtKB.
DR GO; GO:0006210; P:thymine catabolic process; IBA:GO_Central.
DR GO; GO:0019859; P:thymine metabolic process; ISS:UniProtKB.
DR GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
DR GO; GO:0006573; P:valine metabolic process; ISS:UniProtKB.
DR CDD; cd07085; ALDH_F6_MMSDH; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR010061; MeMal-semiAld_DH.
DR PANTHER; PTHR43866; PTHR43866; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01722; MMSDH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Mitochondrion; NAD; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 35..537
FT /note="Methylmalonate-semialdehyde dehydrogenase
FT [acylating], mitochondrial"
FT /id="PRO_0000007188"
FT ACT_SITE 319
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 211..215
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 263..268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 419
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MOD_RES 49
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 49
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 54
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 54
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 57
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 57
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 78
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 78
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 89
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 119
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 119
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 131
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 131
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02252"
FT MOD_RES 300
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 332
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 333
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 366
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 366
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 378
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 378
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02252"
FT MOD_RES 393
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 502
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 519
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT CONFLICT 126..127
FT /note="ML -> TD (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 58063 MW; 69DF39506E62F9C0 CRC64;
MAAVAVAAAA AALRARILQV SSKVNSSWQP ASSFSSSSVP TVKLFIDGKF IESKSDKWID
IHNPATNEVI GRVPESTKAE MDAAVSSCKR TFPAWADTSI LSRQQVLLRY QQLIKENLKE
IARLIMLEQG KTLADAEGDV FRGLQVVEHA CSVTSLMLGD TMPSITKDMD LYSYRLPLGV
CAGIAPFNFP AMIPLWMFPM AMVCGNTFLM KPSERVPGAT MLLAKLFQDS GAPDGTLNII
HGQHEAVNFI CDHPDIKAIS FVGSNQAGEY IFERGSRHGK RVQANMGAKN HGVVMPDANK
ENTLNQLVGA AFGAAGQRCM ALSTAILVGE AKKWLPELVE RAKKLRVNAG DQPGADLGPL
ITPQAKERVC NLIDSGTKEG ASILLDGRSI KVKGYENGNF VGPTIISNVK PNMTCYKEEI
FGPVLVVLET DTLDEAIKIV NDNPYGNGTA IFTTNGATAR KYSHLVDVGQ VGVNVPIPVP
LPMFSFTGSR ASFRGDTNFY GKQGIQFYTQ LKTITSQWKE EDASLSSPAV VMPTMGR
